Data from: Assessment of protein conformation via diazirine-promoted oxidation

Photo-affinity labeling (PAL) utilizes photoreactive molecules to
derivatize proteins in a solvent-accessible dependent manner. The site and
frequency of the products of this reaction can be used to garner insights
into the conformation of the protein. In this work, we document and
characterize a novel oxidation process instigated by UV irradiation of
aromatic diazirines. Diazirine is an increasingly utilized reagent for
probing protein conformations, and this labeling has yet to be documented.
We initially assess the selectivity of the chemical reaction and find that
it is highly selective to methionine (Met) and tryptophan (Trp) residues.
We next examine whether this oxidative labeling can be utilized to
evaluate protein conformation. We assess native and urea-denatured
ubiquitin and cytochrome c, holo- and apo-myoglobin, and native and
copper-bound b-2-microglobulin. In all protein systems but ubiquitin, this
diazirine-promoted oxidation readily differentiates between the two
protein conformations